2QPT
Crystal structure of an EHD ATPase involved in membrane remodelling
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005509 | molecular_function | calcium ion binding |
A | 0005515 | molecular_function | protein binding |
A | 0005524 | molecular_function | ATP binding |
A | 0005525 | molecular_function | GTP binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005768 | cellular_component | endosome |
A | 0005829 | cellular_component | cytosol |
A | 0005886 | cellular_component | plasma membrane |
A | 0005901 | cellular_component | caveola |
A | 0006897 | biological_process | endocytosis |
A | 0010008 | cellular_component | endosome membrane |
A | 0015630 | cellular_component | microtubule cytoskeleton |
A | 0016020 | cellular_component | membrane |
A | 0016787 | molecular_function | hydrolase activity |
A | 0019904 | molecular_function | protein domain specific binding |
A | 0030866 | biological_process | cortical actin cytoskeleton organization |
A | 0032456 | biological_process | endocytic recycling |
A | 0042802 | molecular_function | identical protein binding |
A | 0045171 | cellular_component | intercellular bridge |
A | 0046872 | molecular_function | metal ion binding |
A | 0048471 | cellular_component | perinuclear region of cytoplasm |
A | 0055038 | cellular_component | recycling endosome membrane |
A | 0072659 | biological_process | protein localization to plasma membrane |
A | 0097320 | biological_process | plasma membrane tubulation |
A | 1901741 | biological_process | positive regulation of myoblast fusion |
A | 2001137 | biological_process | positive regulation of endocytic recycling |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MG A 700 |
Chain | Residue |
A | THR72 |
A | THR94 |
A | ANP600 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CA A 701 |
Chain | Residue |
A | ASP494 |
A | ASP496 |
A | ASP498 |
A | MET500 |
A | GLU505 |
site_id | AC3 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE ANP A 600 |
Chain | Residue |
A | SER68 |
A | THR69 |
A | GLY70 |
A | LYS71 |
A | THR72 |
A | SER73 |
A | VAL88 |
A | GLY89 |
A | THR93 |
A | THR94 |
A | GLY156 |
A | ASN219 |
A | LYS220 |
A | SER256 |
A | PHE257 |
A | TRP258 |
A | MG700 |
A | TYR67 |
Functional Information from PROSITE/UniProt
site_id | PS00018 |
Number of Residues | 13 |
Details | EF_HAND_1 EF-hand calcium-binding domain. DVDRDGMLDdeEF |
Chain | Residue | Details |
A | ASP494-PHE506 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:17914359, ECO:0000269|PubMed:24508342, ECO:0007744|PDB:2QPT, ECO:0007744|PDB:4CID |
Chain | Residue | Details |
A | GLY65 | |
A | TRP258 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:24508342, ECO:0007744|PDB:4CID |
Chain | Residue | Details |
A | LYS220 |
site_id | SWS_FT_FI3 |
Number of Residues | 5 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:17914359, ECO:0000269|PubMed:24508342, ECO:0007744|PDB:2QPT, ECO:0007744|PDB:4CID |
Chain | Residue | Details |
A | ASP494 | |
A | ASP496 | |
A | ASP498 | |
A | MET500 | |
A | GLU505 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q4V8H8 |
Chain | Residue | Details |
A | SER3 | |
A | SER493 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:21183079 |
Chain | Residue | Details |
A | SER44 | |
A | SER468 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:15345747, ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079 |
Chain | Residue | Details |
A | SER438 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9NZN4 |
Chain | Residue | Details |
A | SER470 | |
A | SER484 |